Despite an ever-increasing number of high-resolution protein structures, as of 2013, about 40% of protein families had no representative structures, hindering understanding of their function. Ovchinnikov et al. take a step toward filling in this landscape by predicting structures for 58 of the 121 prokaryotic protein families with no known structures. They combined a recent version of Rosetta, which computes structures on the basis of an energy function, with amino acid residue contacts inferred from coevolution patterns in related protein sequences. The authors validated their methods by accurately predicting the structures of two proteins whose structures had previously been solved experimentally.